WNT1_XENLA
ID WNT1_XENLA Reviewed; 371 AA.
AC P10108;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein Wnt-1;
DE Short=XWnt-1;
DE AltName: Full=XInt-1;
DE Flags: Precursor;
GN Name=wnt1; Synonyms=int1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=2911462; DOI=10.1093/nar/17.1.11;
RA Noordermeer J., Meijlink F., Verrijer P., Rijsewijk F., Destree O.;
RT "Isolation of the Xenopus homolog of int-1/wingless and expression during
RT neurula stages of early development.";
RL Nucleic Acids Res. 17:11-18(1989).
RN [2]
RP FUNCTION.
RX PubMed=2673541; DOI=10.1016/0092-8674(89)90506-0;
RA McMahon A.P., Moon R.T.;
RT "Ectopic expression of the proto-oncogene int-1 in Xenopus embryos leads to
RT duplication of the embryonic axis.";
RL Cell 58:1075-1084(1989).
CC -!- FUNCTION: Ligand for members of the frizzled family of seven
CC transmembrane receptors (Probable). Acts in the canonical Wnt signaling
CC pathway by promoting beta-catenin-dependent transcriptional activation
CC (By similarity). Plays an important role in patterning during embryonic
CC development (PubMed:2673541). Plays an essential role in the
CC development of the embryonic brain and central nervous system (CNS) (By
CC similarity). Has a role in osteoblast function, bone development and
CC bone homeostasis (By similarity). {ECO:0000250|UniProtKB:P04426,
CC ECO:0000250|UniProtKB:P04628, ECO:0000269|PubMed:2673541}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P04628}. Secreted
CC {ECO:0000250|UniProtKB:P04628}.
CC -!- TISSUE SPECIFICITY: At neurula in anterior neural fold; at tailbud in
CC dorsal midline of midbrain. {ECO:0000269|PubMed:2911462}.
CC -!- DEVELOPMENTAL STAGE: Neurula onwards. {ECO:0000269|PubMed:2911462}.
CC -!- PTM: Palmitoleoylation is required for efficient binding to frizzled
CC receptors. Palmitoleoylation is necessary for proper trafficking to
CC cell surface (By similarity). Depalmitoleoylated by NOTUM, leading to
CC inhibit Wnt signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:P56704, ECO:0000250|UniProtKB:Q91029}.
CC -!- SIMILARITY: Belongs to the Wnt family. {ECO:0000305}.
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DR EMBL; X13138; CAA31528.1; -; mRNA.
DR PIR; S02113; TVXLT1.
DR RefSeq; NP_001095206.1; NM_001101736.1.
DR AlphaFoldDB; P10108; -.
DR SMR; P10108; -.
DR GeneID; 373578; -.
DR KEGG; xla:373578; -.
DR CTD; 373578; -.
DR Xenbase; XB-GENE-865073; wnt1.L.
DR OrthoDB; 624528at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 373578; Expressed in neurula embryo and 1 other tissue.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0021797; P:forebrain anterior/posterior pattern specification; IMP:DFLAT.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IPI:DFLAT.
DR GO; GO:0014036; P:neural crest cell fate specification; TAS:AgBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2460.20; -; 1.
DR InterPro; IPR005817; Wnt.
DR InterPro; IPR009139; Wnt1.
DR InterPro; IPR043158; Wnt_C.
DR InterPro; IPR018161; Wnt_CS.
DR PANTHER; PTHR12027; PTHR12027; 1.
DR Pfam; PF00110; wnt; 1.
DR PRINTS; PR01841; WNT1PROTEIN.
DR PRINTS; PR01349; WNTPROTEIN.
DR SMART; SM00097; WNT1; 1.
DR PROSITE; PS00246; WNT1; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lipoprotein; Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..371
FT /note="Protein Wnt-1"
FT /id="PRO_0000041409"
FT REGION 261..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 224
FT /note="O-palmitoleoyl serine; by PORCN"
FT /evidence="ECO:0000250|UniProtKB:Q91029"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..104
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 143..151
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 153..170
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 218..232
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 220..227
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 300..331
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 316..326
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 330..370
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 346..361
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 348..358
FT /evidence="ECO:0000250|UniProtKB:P28026"
FT DISULFID 353..354
FT /evidence="ECO:0000250|UniProtKB:P28026"
SQ SEQUENCE 371 AA; 41126 MW; 1FACE4F5F0CB4B72 CRC64;
MRILTFLLGL KTLWVLAFSS LSNTIAVNNS GKWWGIVNVA SAGNVLPGSD ARPVPLVLDP
SLQLLSRQKR LIRQNPGILQ SITRGLHSAI RECKWHFRNR RWNCPTGTGN QVFGKIINRG
CRETAFVFAI TSAGVTHSVA RSCSEGSIES CSCDYRRRGP GGPDWHWGGC SDNIEFGRFI
GREFVDSSER GRDLKYLVNL HNNQAGRLTV LTEMRQECKC HGMSGSCSLR TCWMRLPPFR
SVGDALKDRF DGASKVTYSN NGSNRWGSRS DPPHLEPENP THALPSSQDL VYFEKSPNFC
SPSEKNGTPG TTGRICNSTS LGLDGCELLC CGRGYRSLAE KVTERCHCTF NWCCHVTCLN
CTSSQIVHEC L
